Heat-induced formation of a specific binding site for self-assembled congo red in the V domain of immunoglobulin L chain ?-Reference-Cited by-同舟云学术

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Heat-induced formation of a specific binding site for self-assembled congo red in the V domain of immunoglobulin L chain ?

Published:2001 Issue:6 Volume:59 Page:446-456
ISSN:0006-3525
Container-title:Biopolymers
language:en
Short-container-title:Biopolymers

Author:

Piekarska B.,Konieczny L.,Rybarska J.,Stopa B.,Zemanek G.,Szneler E.,Kr�l M.,Nowak M.,Roterman I.

Publisher

Wiley

Subject

Organic Chemistry,Biomaterials,Biochemistry,General Medicine,Biophysics

Reference61 articles.

1. THE RELATION OF THE PROPERTIES OF CONGO RED-STAINED AMYLOID FIBRILS TO THE β-CONFORMATION

2. From the globular to the fibrous state: protein structure and structural conversion in amyloid formation

3. [1] Staining methods for identification of amyloid in tissue

4. The Acid-Mediated Denaturation Pathway of Transthyretin Yields a Conformational Intermediate That Can Self-Assemble into Amyloid

5. Amyloid fibril formation and protein misassembly: a structural quest for insights into amyloid and prion diseases

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2. Structure and Location of Protein Sites Binding Self-Associated Congo Red Molecules with Intercalated Drugs as Compact Ligands—Theoretical Studies;Biomolecules;2021-03-26

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4. Controlled Release of Doxorubicin from the Drug Delivery Formulation Composed of Single-Walled Carbon Nanotubes and Congo Red: A Molecular Dynamics Study and Dynamic Light Scattering Analysis;Pharmaceutics;2020-07-03

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